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The Hsp60 Protein of Helicobacter Pylori Exhibits Chaperone and ATPase Activities at Elevated Temperatures

Department of Chemistry and Biochemistry, California State University, San Marcos, CA 92096, USA
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Author to whom correspondence should be addressed.
Academic Editor: Yehia Mechref
Received: 2 March 2021 / Revised: 24 March 2021 / Accepted: 30 March 2021 / Published: 3 April 2021
The heat-shock protein, Hsp60, is one of the most abundant proteins in Helicobacter pylori. Given its sequence homology to the Escherichia coli Hsp60 or GroEL, Hsp60 from H. pylori would be expected to function as a molecular chaperone in this organism. H. pylori is a type of bacteria that grows on the gastric epithelium, where the pH can fluctuate between neutral and 4.5, and the intracellular pH can be as low as 5.0. We previously showed that Hsp60 functions as a chaperone under acidic conditions. However, no reports have been made on the ability of Hsp60 to function as a molecular chaperone under other stressful conditions, such as heat stress or elevated temperatures. We report here that Hsp60 could suppress the heat-induced aggregation of the enzymes rhodanese, malate dehydrogenase, citrate synthase, and lactate dehydrogenase. Moreover, Hsp60 was found to have a potassium and magnesium-dependent ATPase activity that was stimulated at elevated temperatures. Although, Hsp60 was found to bind GTP, the hydrolysis of this nucleotide could not be observed. Our results show that Hsp60 from H. pylori can function as a molecular chaperone under conditions of heat stress. View Full-Text
Keywords: Hsp60; molecular chaperone; protein aggregation; heat stress Hsp60; molecular chaperone; protein aggregation; heat stress
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MDPI and ACS Style

Mendoza, J.A.; Ignacio, J.L.; Buckley, C.M. The Hsp60 Protein of Helicobacter Pylori Exhibits Chaperone and ATPase Activities at Elevated Temperatures. BioChem 2021, 1, 19-25. https://0-doi-org.brum.beds.ac.uk/10.3390/biochem1010002

AMA Style

Mendoza JA, Ignacio JL, Buckley CM. The Hsp60 Protein of Helicobacter Pylori Exhibits Chaperone and ATPase Activities at Elevated Temperatures. BioChem. 2021; 1(1):19-25. https://0-doi-org.brum.beds.ac.uk/10.3390/biochem1010002

Chicago/Turabian Style

Mendoza, Jose A., Julian L. Ignacio, and Christopher M. Buckley 2021. "The Hsp60 Protein of Helicobacter Pylori Exhibits Chaperone and ATPase Activities at Elevated Temperatures" BioChem 1, no. 1: 19-25. https://0-doi-org.brum.beds.ac.uk/10.3390/biochem1010002

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